@article{Doucey2003Integ-36626,
  year={2003},
  doi={10.1074/jbc.M302709200},
  title={The β1 and β3 Integrins Promote T Cell Receptor-mediated Cytotoxic T Lymphocyte Activation},
  number={29},
  volume={278},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={26983--26991},
  author={Doucey, Marie-Agnès and Legler, Daniel F. and Faroudi, Mustapha and Boucheron, Nicole and Baumgaertner, Petra and Naeher, Dieter and Cebecauer, Marek and Hudrisier, Denis and Rüegg, Curzio and Luescher, Immanuel F.}
}

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    <dc:creator>Legler, Daniel F.</dc:creator>
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    <dcterms:abstract xml:lang="eng">Recognition by CD8&lt;sup&gt;+&lt;/sup&gt; cytotoxic T lymphocytes (CTLs) of antigenic peptides bound to major histocompatibility class (MHC) I molecules on target cells leads to sustained calcium mobilization and CTL degranulation resulting in perforin-dependent killing. We report that beta&lt;sub&gt;1&lt;/sub&gt; and beta&lt;sub&gt;3&lt;/sub&gt; integrin-mediated adhesion to extracellular matrix proteins on target cells and/or surfaces dramatically promotes CTL degranulation. CTLs, when adhered to fibronectin but not CTL in suspension, efficiently degranulate upon exposure to soluble MHC.peptide complexes, even monomeric ones. This adhesion induces recruitment and activation of the focal adhesion kinase Pyk2, the cytoskeleton linker paxillin, and the Src kinases Lck and Fyn in the contact site. The T cell receptor, by association with Pyk2, becomes part of this adhesion-induced activation cluster, which greatly increases its signaling.</dcterms:abstract>
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